ID W3WMB0_PESFW Unreviewed; 506 AA.
AC W3WMB0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Amidohydrolase-related domain-containing protein {ECO:0000259|Pfam:PF01979};
GN ORFNames=PFICI_13383 {ECO:0000313|EMBL:ETS74899.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS74899.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
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DR EMBL; KI912119; ETS74899.1; -; Genomic_DNA.
DR RefSeq; XP_007840155.1; XM_007841964.1.
DR AlphaFoldDB; W3WMB0; -.
DR STRING; 1229662.W3WMB0; -.
DR GeneID; 19278396; -.
DR KEGG; pfy:PFICI_13383; -.
DR eggNOG; ENOG502RKQ5; Eukaryota.
DR HOGENOM; CLU_538724_0_0_1; -.
DR InParanoid; W3WMB0; -.
DR OMA; AKVVWSP; -.
DR OrthoDB; 1767076at2759; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43794:SF11; AMIDOHYDRO-REL DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43794; AMINOHYDROLASE SSNA-RELATED; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030651};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 288..439
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 506 AA; 54815 MW; D6CCE16EE4599EBF CRC64;
MTLVRRRAKA LWIYAIIIVF FAFCLFLARR FLPNSSFSNI LFGSVSHGGC KIITKGNYDK
LILKGVVLTP KGPLQDGYVL VESGKVAEVG TSYSSESQDT LITVVDCANS VISPGFINLH
EHLTYSIVSP FKDLGERVSH RHDWRVGARN RTIREALVAE DMIGDSIKWG ELRHLFSGTT
SVVGGGMVTG LVRNLDFASG LEAGLLDAPS VWDVFPLDDA DGILRNNDCD YGPEAIDRQR
AEKYHRYLAH VGEGVDDEAA NEFRCLSDET YDSLPMPGGG GLSTDIIAPN LAMVHALGLS
ASDFDLVAKR GAHIIWSPRS NMFLYGKTLN ITYLLEAGIN VALGTDWLPS GSATMSREAH
CAALATQQLY GRHLEAKTIW EMMTINAARA ASFEQHIGSL EVGKLADIVI FTESTGDVYS
QAVFGSTENI EMVLRGGRVL LVGDKLGGLS SSHCEPVQIG RSRKAICIAD ELGLSYAEFA
ASLAGFYPAA LPSIPPYEPL CDAIVS
//
